94280
Urease from Canavalia ensiformis (Jack bean)
powder, ~1 U/mg
Synonym(s):
Jack bean urease, Urea amidohydrolase
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About This Item
CAS Number:
UNSPSC Code:
12352204
eCl@ss:
32160410
EC Number:
232-656-0
NACRES:
NA.54
MDL number:
Specific activity:
~1 U/mg
General description
Urease (Ure) enzyme is present in the cytosol. It is active at acidic pH and is expressed at 28°C. Urease consists of nickel and is present in archaea, bacteria, unicellular eukaryotes and plants.
Subunit molecular weight: ~90,770
Composed of six subunits with total molecular weight: ~544,620
Composed of six subunits with total molecular weight: ~544,620
Application
Urease from Canavalia ensiformis (Jack bean) has been used in purification and crystallization studies.
Urease from Canavalia ensiformis may be used for urea determination of various samples, such as legumes . It may be useful for the detection of pathogens as well as heavy-metal ions.
Biochem/physiol Actions
Urease catalyzes the hydrolysis of urea into carbon dioxide and ammonia. Urease is involved in nitrogen metabolism and urea degradation. Urease from Canavalia ensiformis binds 2 nickel ions per subunit .
Other Notes
1 U corresponds to the amount of enzyme which hydrolyzes 1 μmol urea (Cat. No. 51459) per minute at pH 8.0 and 25 °C.
Application in (selective) hydrolysis/condensations;citation structure.
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signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk
WGK 1
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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I.A. Natchev
Tetrahedron, 44, 1511-1511 (1988)
M J Sculley et al.
Biophysical chemistry, 19(1), 39-47 (1984-01-01)
The use of bifunctional reagents to form cross-links between subunits in protein oligomers and subsequent disruption of noncovalent interactions with SDS allows comment upon the number of subunits and the symmetry in the original assembly. In existing treatments the number
Isothermal titration calorimetry to characterize enzymatic reactions
Methods in Enzymology, 567, 215-236 (2016)